Immunoprecipitation is a traditional approach to isolate single proteins or native protein complexes from a complex sample mixture. The original method makes use of specific antibodies against endogenous proteins or epitope tags, which are first bound to the target protein and then isolated with protein A beads. An advancement of this method is the application of a protein A tag fused to the target protein and the affinity-purification of the tagged protein with human Immunoglobulin G chemically cross-linked to a sepharose matrix. This method will be described exemplified by the purification of protein complexes of the peroxisomal membrane from yeast Saccharomyces cerevisiae.
CITATION STYLE
Hansen, T., Chan, A., Schröter, T., Schwerter, D., Girzalsky, W., & Erdmann, R. (2017). Isolation of native soluble and membrane-bound protein complexes from yeast Saccharomyces cerevisiae. In Methods in Molecular Biology (Vol. 1595, pp. 37–44). Humana Press Inc. https://doi.org/10.1007/978-1-4939-6937-1_4
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